Molecular importance of prawn large heat shock proteins 60, 70 and 90

Chaurasia MK 1 , Nizam F 1 , Ravichandran G 2 , Arasu MV 3 , Al-Dhabi NA 3 , Arshad A 4 Show all authors , Elumalai P 5 , Arockiaraj J 6

Affiliations 

  • 1 Division of Fisheries Biotechnology & Molecular Biology, Department of Biotechnology, Faculty of Science and Humanities, SRM University, Kattankulathur, 603 203, Chennai, Tamil Nadu, India
  • 2 Division of Fisheries Biotechnology & Molecular Biology, Department of Biotechnology, Faculty of Science and Humanities, SRM University, Kattankulathur, 603 203, Chennai, Tamil Nadu, India; SRM Research Institute, SRM University, Kattankulathur, 603 203, Chennai, Tamil Nadu, India
  • 3 Department of Botany and Microbiology, Addiriyah Chair for Environmental Studies, College of Science, King Saud University, P. O. Box 2455, Riyadh, 11451, Saudi Arabia
  • 4 Department of Aquaculture, Faculty of Agriculture, Universiti Putra Malaysia, 43400, UPM, Serdang, Selangor, Malaysia
  • 5 School of Aquatic Food Products and Technology, Kerala University of Fisheries and Ocean Studies, Panangad, Kochi, 682 506, Kerala, India
  • 6 Division of Fisheries Biotechnology & Molecular Biology, Department of Biotechnology, Faculty of Science and Humanities, SRM University, Kattankulathur, 603 203, Chennai, Tamil Nadu, India. Electronic address: jesuaraj@hotmail.com
Fish Shellfish Immunol, 2016 Jan;48:228-38.
PMID: 26631804 DOI: 10.1016/j.fsi.2015.11.034

Abstract

Considering the importance of heat shock proteins (HSPs) in the innate immune system of prawn, a comparative molecular approach was proposed to study the crustacean large HSPs 60, 70 and 90. Three different large HSPs were identified from freshwater prawn Macrobrachium rosenbergii (Mr) cDNA library during screening. The structural and functional characteristic features of HSPs were studied using various bioinformatics tools. Also, their gene expression and mRNA regulation upon various pathogenic infections was studied by relative quantification using 2(-ΔΔCT) method. MrHSP60 contains a long chaperonin 60 domain at 46-547 which carries a chaperonin 60 signature motif between 427 and 438, whereas MrHSP70 contains a long HSP70 domain at 21-624 and MrHSP90 carries a HSP90 domain at 188-719. The two dimensional analysis showed that MrHSP60 contains more amino acids (52%) in helices, whereas MrHSP70 (40.6%) and MrHSP90 (51.8%) carried more residues in coils. Gene expression results showed significant (P 

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